Tyrosine 263 in cyanobacterial phytochrome Cph1 optimizes photochemistry at the prelumi-R→lumi-R step

Vitaly Sineshchekov, Joel Mailliet, Georgios Psakis, Kathleen Feilke, Jakub Kopycki, Mathias Zeidler, Lars Oliver Essen, Jon Hughes

Research output: Contribution to journalArticle

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Abstract

We report a low-temperature fluorescence spectroscopy study of the PAS-GAF-PHY sensory module of Cph1 phytochrome, its Y263F mutant (both with known 3D structures) as well as Y263H and Y263S to connect their photochemical parameters with intramolecular interactions. None of the holoproteins showed photochemical activity at low temperature, and the activation barriers for the Pr→lumi-R photoreaction (2.5–3.1 kJ mol−1) and fluorescence quantum yields (0.29–0.42) were similar. The effect of the mutations on Pr→Pfr photoconversion efficiency (ΦPr→Pfr) was observed primarily at the prelumi-R S0 bifurcation point corresponding to the conical intersection of the energy surfaces at which the molecule relaxes to form lumi-R or Pr, lowering ΦPr→Pfr from 0.13 in the wild type to 0.05–0.07 in the mutants. We suggest that the Eaactivation barrier in the Pr* S1 excited state might correspond to the D-ring (C19) carbonyl – H290 hydrogen bond or possibly to the hindrance caused by the C131/C171 methyl groups of the C and D rings. The critical role of the tyrosine hydroxyl group can be at the prelumi-R bifurcation point to optimize the yield of the photoprocess and energy storage in the form of lumi-R for subsequent rearrangement processes culminating in Pfr formation.
LanguageEnglish
Pages786-795
Number of pages10
JournalPhotochemistry and Photobiology
Volume90
Issue number4
Early online date28 Mar 2014
DOIs
Publication statusPublished - Jul 2014
Externally publishedYes

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phytochrome
Phytochrome
Photochemistry
Photochemical reactions
tyrosine
photochemical reactions
Tyrosine
PAS
fluorescence
Temperature
rings
Fluorescence Spectrometry
Fluorescence spectroscopy
Quantum yield
energy storage
mutations
Interfacial energy
Excited states
Hydroxyl Radical
Energy storage

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Sineshchekov, Vitaly ; Mailliet, Joel ; Psakis, Georgios ; Feilke, Kathleen ; Kopycki, Jakub ; Zeidler, Mathias ; Essen, Lars Oliver ; Hughes, Jon. / Tyrosine 263 in cyanobacterial phytochrome Cph1 optimizes photochemistry at the prelumi-R→lumi-R step. In: Photochemistry and Photobiology. 2014 ; Vol. 90, No. 4. pp. 786-795.
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abstract = "We report a low-temperature fluorescence spectroscopy study of the PAS-GAF-PHY sensory module of Cph1 phytochrome, its Y263F mutant (both with known 3D structures) as well as Y263H and Y263S to connect their photochemical parameters with intramolecular interactions. None of the holoproteins showed photochemical activity at low temperature, and the activation barriers for the Pr→lumi-R photoreaction (2.5–3.1 kJ mol−1) and fluorescence quantum yields (0.29–0.42) were similar. The effect of the mutations on Pr→Pfr photoconversion efficiency (ΦPr→Pfr) was observed primarily at the prelumi-R S0 bifurcation point corresponding to the conical intersection of the energy surfaces at which the molecule relaxes to form lumi-R or Pr, lowering ΦPr→Pfr from 0.13 in the wild type to 0.05–0.07 in the mutants. We suggest that the Eaactivation barrier in the Pr* S1 excited state might correspond to the D-ring (C19) carbonyl – H290 hydrogen bond or possibly to the hindrance caused by the C131/C171 methyl groups of the C and D rings. The critical role of the tyrosine hydroxyl group can be at the prelumi-R bifurcation point to optimize the yield of the photoprocess and energy storage in the form of lumi-R for subsequent rearrangement processes culminating in Pfr formation.",
author = "Vitaly Sineshchekov and Joel Mailliet and Georgios Psakis and Kathleen Feilke and Jakub Kopycki and Mathias Zeidler and Essen, {Lars Oliver} and Jon Hughes",
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Sineshchekov, V, Mailliet, J, Psakis, G, Feilke, K, Kopycki, J, Zeidler, M, Essen, LO & Hughes, J 2014, 'Tyrosine 263 in cyanobacterial phytochrome Cph1 optimizes photochemistry at the prelumi-R→lumi-R step', Photochemistry and Photobiology, vol. 90, no. 4, pp. 786-795. https://doi.org/10.1111/php.12263

Tyrosine 263 in cyanobacterial phytochrome Cph1 optimizes photochemistry at the prelumi-R→lumi-R step. / Sineshchekov, Vitaly; Mailliet, Joel; Psakis, Georgios; Feilke, Kathleen; Kopycki, Jakub; Zeidler, Mathias; Essen, Lars Oliver; Hughes, Jon.

In: Photochemistry and Photobiology, Vol. 90, No. 4, 07.2014, p. 786-795.

Research output: Contribution to journalArticle

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T1 - Tyrosine 263 in cyanobacterial phytochrome Cph1 optimizes photochemistry at the prelumi-R→lumi-R step

AU - Sineshchekov, Vitaly

AU - Mailliet, Joel

AU - Psakis, Georgios

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AU - Kopycki, Jakub

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AU - Essen, Lars Oliver

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